Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00361
Entry Name
UniProt Accession
Theoretical PI
4.73
Molecular Weight
20615.46
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Rap-2a
Protein Synonyms/Alias
RbBP-30;
Gene Name
RAP2A
Gene Synonyms/Alias
Created Date
01-JUL-1989
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
176
Canonical
QPDKDDPCCSACNIQ
[1]
S-Palmitoylation
177
Canonical
PDKDDPCCSACNIQ*
[1]
S-Palmitoylation
180
Canonical
DDPCCSACNIQ****
[2]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
[2] Farrell FX, Yamamoto K, Lapetina EG. Prenyl group identification of rap2proteins: a ras superfamily member other than ras that is farnesylated. BiochemJ. 1993 Jan 15;289 ( Pt 2):349-55.[PMID:8424780]
Functional Description
Small GTP-binding protein which cycles between a GDP- bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading.
Sequence Annotation
Nucleotide-binding: 10 17 GTP.
Nucleotide-binding: 57 61 GTP.
Nucleotide-binding: 116 119 GTP.
Motif: 32 40 Effector region.
Modified residue: 180 180 Cysteine methyl ester.
Protein Length
183 AA.
Protein Sequence
(Canonical)
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG  60
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYEKVP VILVGNKVDL  120
ESEREVSSSE GRALAEEWGC PFMETSAKSK TMVDELFAEI VRQMNYAAQP DKDDPCCSAC  180
NIQ                                                                183
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG  60
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYEKVP VILVGNKVDL  120
ESEREVSSSE GRALAEEWGC PFMETSAKSK TMVDELFAEI VRQMNYAAQP DKDDPCCSAC  180
NIQ                                                                183
FASTA
(Canonical)
>LipidDB-9606-00361|P10114
MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAG
TEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDL
ESEREVSSSEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSAC
NIQ
MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAG
TEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDL
ESEREVSSSEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSAC
NIQ
Gene Ontology
GO:0005829; C:cytosol; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0055037; C:recycling endosome; IDA:MGI
GO:0055038; C:recycling endosome membrane; IDA:UniProtKB
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IDA:UniProtKB
GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB
GO:0034613; P:cellular protein localization; IDA:UniProtKB
GO:0045184; P:establishment of protein localization; IDA:MGI
GO:0030336; P:negative regulation of cell migration; IEA:Ensembl
GO:0031954; P:positive regulation of protein autophosphorylation; IDA:UniProtKB
GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB
GO:0048814; P:regulation of dendrite morphogenesis; IDA:UniProtKB
GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR020849; Small_GTPase_Ras
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00173; RAS;
PROSITE
PROSITE; PS51421; RAS;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;